BMRB Entry 15329

Name: Solution NMR structure of Tubulin polymerization-promoting protein family member 3 from Homo sapiens. Northeast Structural Genomics target HR387.
Published: 2007-07-19

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PDB ID: 2jrf
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15329
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR structure of Tubulin polymerization-promoting protein family member 3 from Homo sapiens. Northeast Structural Genomics target HR387.

Deposition date:

2007-06-25

Original release date:

2007-07-19

Authors:

Aramini, James; Rossi, Paolo; Shastry, Ritu; Nwosu, Chioma; Cunningham, Kellie; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Rajan, P.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano

Citation:

Citation: Aramini, James; Rossi, Paolo; Shastry, Ritu; Nwosu, Chioma; Cunningham, Kellie; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Rajan, P.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano. "Solution NMR structure of Tubulin polymerization-promoting protein family member 3 from Homo sapiens. Northeast Structural Genomics target HR387." .
PubMed: TBA

Assembly members:

Assembly members:
hr387, polymer, 184 residues, 20075.820 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: HR387-21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hr387: MAASTDIAGLEESFRKFAIH GDPKASGQEMNGKNWAKLCK DCKVADGKSVTGTDVDIVFS KVKGKSARVINYEEFKKALE ELATKRFKGKSKEEAFDAIC QLVAGKEPANVGVTKAKTGG AVDRLTDTSRYTGSHKERFD ESGKGKGIAGRQDILDDSGY VSAYKNAGTYDAKVKKLEHH HHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	755
15N chemical shifts	179
1H chemical shifts	1114

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hr387	1

Entities:

Entity 1, hr387 184 residues - 20075.820 Da.

Sequence has a M7I mutation. Residues 177-184 constitute a non-native affinity purification tag (LEHHHHHH)

1

MET

ALA

SER

THR

ASP

ILE

ALA

GLY

LEU

2

GLU

SER

PHE

ARG

LYS

PHE

ALA

ILE

HIS

3

GLY

ASP

PRO

LYS

ALA

SER

GLY

GLN

GLU

MET

4

ASN

GLY

LYS

ASN

TRP

ALA

LYS

LEU

CYS

LYS

5

ASP

CYS

LYS

VAL

ALA

ASP

GLY

LYS

SER

VAL

6

THR

GLY

THR

ASP

VAL

ASP

ILE

VAL

PHE

SER

7

LYS

VAL

LYS

GLY

LYS

SER

ALA

ARG

VAL

ILE

8

ASN

TYR

GLU

PHE

LYS

ALA

LEU

GLU

9

GLU

LEU

ALA

THR

LYS

ARG

PHE

LYS

GLY

LYS

10

SER

LYS

GLU

ALA

PHE

ASP

ALA

ILE

CYS

11

GLN

LEU

VAL

ALA

GLY

LYS

GLU

PRO

ALA

ASN

12

VAL

GLY

VAL

THR

LYS

ALA

LYS

THR

GLY

13

ALA

VAL

ASP

ARG

LEU

THR

ASP

THR

SER

ARG

14

TYR

THR

GLY

SER

HIS

LYS

GLU

ARG

PHE

ASP

15

GLU

SER

GLY

LYS

GLY

LYS

GLY

ILE

ALA

GLY

16

ARG

GLN

ASP

ILE

LEU

ASP

SER

GLY

TYR

17

VAL

SER

ALA

TYR

LYS

ASN

ALA

GLY

THR

TYR

18

ASP

ALA

LYS

VAL

LYS

LEU

GLU

HIS

19

HIS

Samples:

sample_1: hr387, [U-100% 13C; U-100% 15N], 1.04 mM; ammonium acetate 20 mM; sodium chloride 100 mM; DTT 10 mM; calcium chloride 5 mM; sodium azide 0.02%; H2O 95%; D2O 5%

sample_2: hr387, [U-5% 13C; U-100% 15N], 0.7 mM; ammonium acetate 20 mM; calcium chloride 100 mM; DTT 10 mM; calcium chloride 5 mM; sodium azide 0.02%; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 100 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY aromatic	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC high res.	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection

AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

SPARKY v3.110, Goddard - data analysis, peak picking

AutoStruct v2.1.1, Huang, Tejero, Powers and Montelione - structure solution

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

X-PLOR NIH v2.11.2, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

PSVS v1.3, Bhattacharya and Montelione - data analysis, structure validation

PDBStat v5.0, Tejero and Montelione - PDB analysis

TALOS, Cornilescu, Delaglio and Bax - dihedral angle constraints

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz

PDB	2JRF
DBJ	BAB26493 BAB28237 BAE32991 BAE35831
GB	AAD27747 AAH00691 AAH10788 ADQ33176 AIC51554
REF	NP_001181772 NP_057048 NP_057224 NP_080757 XP_001496480
SP	Q9BW30 Q9CRB6
AlphaFold	Q9BW30 Q9CRB6